Proteomic Analysis of Salicylate-Induced Proteins of Pea (Pisum sativum L.) Leaves

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I. A. Tarchevsky, V. G. Yakovleva^*, and A. M. Egorova

Kazan Institute of Biochemistry and Biophysics, Kazan Research Center, Russian Academy of Sciences, ul. Lobachevskogo 2/31, 420111 Kazan, Russia; fax: (843) 292-7347; E-mail: tarchevsky@mail.knc.ru

^* To whom correspondence should be addressed.

Received November 14, 2008; Revision received April 1, 2009

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The effect of 50 µM salicylic acid on soluble proteins of pea (Pisum sativum L.) leaves was studied by proteomic analysis. Thirty-two salicylate-induced proteins were found, and 13 of these were identified using MALDI TOF MS. Salicylate-induced increased content was shown for the first time for the family 18 glycoside hydrolase, α-amylase, 33 kDa protein of photosystem II, lipid-desaturase-like protein, and glutamine amidotransferase. Increased content of protective proteins of direct antipathogenic action such as chitinase and β-1,3-glucanases was also noted.

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KEY WORDS: salicylic acid, proteomic investigations, salicylate-induced proteins

DOI: 10.1134/S0006297910050081

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